Regulation of myosin and filamentous actin interaction by tropomyosin is a central feature of
contractile events in muscle and nonmuscle cells. However, little is known about molecular …

Tropomyosin is present in virtually all eucaryotic cells, where it functions to modulate actin-
myosin interaction and to stabilize actin filament structure. In striated muscle, tropomyosin …

Tropomyosin is a coiled-coil protein that binds head-to-tail along the length of actin filaments
in eukaryotic cells, stabilizing them and providing protection from severing proteins …

The motor protein myosin drives muscle and nonmuscle motility by binding to and moving
along actin of thin filaments. Myosin binding to actin also modulates interactions of the …

Previous work has shown that there are significant differences in the X-ray diffraction
patterns obtained from relaxed and contracting muscles. We show that some of these …

Abstract Analysis of the periodic distribution of amino acids in tropomyosin has revealed the
presence of seven or 14 quasi-equivalent actin-binding sites. We tested the hypothesis of …

The crystal structure of tropomyosin filaments has been solved to 15 Å resolution by
refinement of models against the diffraction data and heavy atom labeling of cysteine …

Cooperative myosin binding to the thin filament is critical to regulation of cardiac and
skeletal muscle contraction. This report delineates and fits to experimental data a new model …

Head-to-tail polymerization of tropomyosin is crucial for its actin binding, function in actin
filament assembly, and the regulation of actin-myosin contraction. Here, we describe the 2.1 …

Tropomyosin is a two-chain α-helical coiled coil whose periodic interactions with the F-actin
helix are critical for thin filament stabilization and the regulation of muscle contraction. Here …